- Sulfation of various alcoholic groups by an arylsulfate sulfotransferase from Desulfitobacterium hafniense and synthesis of estradiol sulfate
- Advanced Synthesis & Catalysis
- Volume | Issue number
- 354 | 18
- Pages (from-to)
- Document type
- Faculty of Science (FNWI)
- Van 't Hoff Institute for Molecular Sciences (HIMS)
Bacterial arylsulfate sulfotransferases (AST) are enzymes that catalyse the transfer of a sulfate group from p-nitrophenyl sulfate (p-NPS) to a phenolic acceptor molecule. By screening of the NCBI protein database a gene coding for an AST was found in Desulfitobacterium hafniense. After expression the enzyme was purified and characterised. This AST efficiently sulfates various acceptor molecules (estrone, estradiol, enkephalin and non-phenolic alcohols) using p-NPS as sulfate donor. The purified AST has a pH optimum of 9.6, it is stable in the presence of 10% of DMSO, and depending on the conditions it has a melting temperature of up to 47 °C. Surprisingly, and in great contrast to all other known bacterial ASTs, this enzyme was able to use a variety of non-phenolic alcohols as sulfate acceptor. Because of these properties, this unique enzyme is a promising tool for biotransformation processes, providing a green and simple method to specifically sulfate compounds without need for functional group protection.
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